N-terminal amino acid sequences of troponin T fragments, including 30 kDa one, produced during postmortem aging of bovine longissimus muscle
Author:
Publisher
Elsevier BV
Subject
Food Science
Reference19 articles.
1. N-terminal amino acid sequences of three functionally different troponin T isoforms from rabbit fast skeletal muscle;Briggs;Journal of Molecular Biology,1989
2. Identification of the 30 kDa polypeptide in post mortem skeletal muscle as a degradation product of troponin-T;Ho;Biochimie,1994
3. Factors contributing to proteolysis and distribution of myofibrillar proteins and the impact on tenderization in beef and sheep meat;Hopkins;Australian Journal of Agricultural Research,2002
4. Proteolysis of specific muscle structural proteins by m-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle;Huff-Lonergan;Journal of Animal Science,1996
5. Characterization of peptides related from rabbit skeletal muscle troponin-T by μ-calpain under conditions of low temperature and high ionic strength;Hughes;Meat Science,2001
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